Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA2981
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA2981 lpxK
Status: annotated
Amino acids: 332
Structure source: AlphaFold

EC

2.7.1.130

GO

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. GO:0009029 Catalysis of the reaction: a lipid A disaccharide + ATP = a lipid IVA + ADP + H+. GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common. GO:0009244 The chemical reactions and pathways resulting in the formation of the core region of bacterial lipopolysaccharides, which contains ten saccharide residues.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Gut microbiome off-target: hit
Essential (DEG): Y
Localization: Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.641

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

MSFSERLLAAWYQGHPALALLRPLEALYRRVANGRRADFLSGRKPAYRAPLPVLVVGNITVGGTGKTPMILWMIEHCRARGLRVGVISRGYGARPPTTPWRVRAEQDAAEAGDEPLMIVRRSGVPLMIDPDRPRALQALLAEEQLDLVLCDDGLQHYRLARDLELVLIDAARGLGNGRCLPAGPLREPAERLESVDALLYNGADEDPDGGYAFRLQPTALINLQSGERRPLEHFPAGQEVHALAGIGNPQRFFRTLEALHWRAIPHAFPDHATYTAAELAFSPPLPLLMTEKDAVKCRAFAAADWWYLAVDAVPSPAFVAWFDARLEHLLAR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

2.7.1.130

Gene Ontology (GO)

5

GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0009029 Catalysis of the reaction: a lipid A disaccharide + ATP = a lipid IVA + ADP + H+.
GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
GO:0009244 The chemical reactions and pathways resulting in the formation of the core region of bacterial lipopolysaccharides, which contains ten saccharide residues.

Sequence Features

Domain/signature hits from InterPro and related databases.

10 records

Show feature table

Start	End	DB	Term	Name
3	331	Hamap	MF_00409	Tetraacyldisaccharide 4'-kinase [lpxK].
3	331	InterPro	IPR003758	Tetraacyldisaccharide 4'-kinase
53	191	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
53	191	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
19	326	Pfam	PF02606	Tetraacyldisaccharide-1-P 4'-kinase
19	326	InterPro	IPR003758	Tetraacyldisaccharide 4'-kinase
15	330	PANTHER	PTHR42724	TETRAACYLDISACCHARIDE 4'-KINASE
15	330	InterPro	IPR003758	Tetraacyldisaccharide 4'-kinase
27	313	NCBIfam	TIGR00682	tetraacyldisaccharide 4'-kinase
27	313	InterPro	IPR003758	Tetraacyldisaccharide 4'-kinase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold PA2981	AlphaFold	—	—	full sequence	—	Viewing

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
1				0.641

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

2 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
LP4	4LKV	O67572	711.9 Da LogP 4.91 TPSA 212.3	2 viol.	✓ Clean	`CCCCCCCCCCC[C@H](CC(=O)N[C@@H]1[C@H]([C@@H]([C@…`
LP5	4LKV	O67572	711.9 Da LogP 4.91 TPSA 212.3	2 viol.	✓ Clean	`CCCCCCCCCCC[C@H](CC(=O)N[C@@H]1[C@H]([C@@H]([C@…`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

No virtual-screening candidates for this protein.

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

PA2981